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http://purl.uniprot.org/citations/30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30623173http://www.w3.org/2000/01/rdf-schema#comment"Cyclin G-associated kinase (GAK) is a ubiquitous serine/threonine kinase that facilitates clathrin uncoating during vesicle trafficking. GAK phosphorylates a coat adaptor component, AP2M1, to help achieve this function. GAK is also implicated in Parkinson's disease through genome-wide association studies. However, GAK's role in mammalian neurons remains unclear, and insight may come from identification of further substrates. Employing a chemical genetics method, we show here that the sodium potassium pump (Na+/K+-ATPase) α-subunit Atp1a3 is a GAK target and that GAK regulates Na+/K+-ATPase trafficking to the plasma membrane. Whole-cell patch clamp recordings from CA1 pyramidal neurons in GAK conditional knockout mice show a larger change in resting membrane potential when exposed to the Na+/K+-ATPase blocker ouabain, indicating compromised Na+/K+-ATPase function in GAK knockouts. Our results suggest a modulatory role for GAK via phosphoregulation of substrates such as Atp1a3 during cargo trafficking."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.org/dc/terms/identifier"doi:10.26508/lsa.201800118"xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"George R."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Snijders A.P."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Flynn H."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Lin A.W."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Gill K.K."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Claxton S."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Ultanir S.K."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Castaneda M.S."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Eder N."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/author"Matucci I."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/name"Life Sci Alliance"xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/pages"e201800118"xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/title"Chemical genetic identification of GAK substrates reveals its role in regulating Na+/K+-ATPase."xsd:string
http://purl.uniprot.org/citations/30623173http://purl.uniprot.org/core/volume"1"xsd:string
http://purl.uniprot.org/citations/30623173http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30623173
http://purl.uniprot.org/citations/30623173http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30623173
http://purl.uniprot.org/uniprot/#_A0A0G2JFZ0-mappedCitation-30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30623173
http://purl.uniprot.org/uniprot/#_A0A0G2JGP6-mappedCitation-30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30623173
http://purl.uniprot.org/uniprot/#_A0A0R4J0F6-mappedCitation-30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30623173
http://purl.uniprot.org/uniprot/#_A0A0G2JEW6-mappedCitation-30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30623173
http://purl.uniprot.org/uniprot/#_P48986-mappedCitation-30623173http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30623173